TY  - JOUR
AU  - Izrael‑Živković, Lidija
AU  - Gojgić-Cvijović, Gordana
AU  - Gopcevic, K.R.
AU  - Vrvić, Miroslav
AU  - Karadžić, Ivanka
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/587
AB  - An extracellular lipase from Pseudomonas aeruginosa ATCC 27853 has been purified and its enzymatic characteristics were determined. According to SDS-PAGE and gel filtration molecular mass estimated to be 30 kDa, what classified the lipase in group I.1. Although 14 lipases from P. aeruginosa with similar molecular mass are referred to date, their basic enzymatic properties have not been reported yet. To address the gap we found: the optimal temperature and pH in water solution being 50 °C and 9.3, respectively; the lipase was inhibited with Hg2+ ions and sodium dodecylsulphate (SDS), while non-ionic detergent Triton X-100 activated the enzyme; the lipase hydrolyzed more rapidly middle chain triglycerides and it was not regiospecific; the lipase demonstrated naturally occurring stability in different organic solvents with concentrations ranging from 30 to 70%, including good thermal stability in 30% organic solvent solution. Even though strain P. aeruginosa ATCC 27853 was not isolated from extreme environment it showed activity in organic solvent suggesting that this lipase is suitable for variety of applications, including reactions in water restricted medium and bioremediation of contaminations by organic solvents.
T2  - Journal of Basic Microbiology
T1  - Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853
VL  - 49
IS  - 5
SP  - 452
EP  - 462
DO  - 10.1002/jobm.200800229
ER  - 

@article{
author = "Izrael‑Živković, Lidija and Gojgić-Cvijović, Gordana and Gopcevic, K.R. and Vrvić, Miroslav and Karadžić, Ivanka",
year = "2009",
abstract = "An extracellular lipase from Pseudomonas aeruginosa ATCC 27853 has been purified and its enzymatic characteristics were determined. According to SDS-PAGE and gel filtration molecular mass estimated to be 30 kDa, what classified the lipase in group I.1. Although 14 lipases from P. aeruginosa with similar molecular mass are referred to date, their basic enzymatic properties have not been reported yet. To address the gap we found: the optimal temperature and pH in water solution being 50 °C and 9.3, respectively; the lipase was inhibited with Hg2+ ions and sodium dodecylsulphate (SDS), while non-ionic detergent Triton X-100 activated the enzyme; the lipase hydrolyzed more rapidly middle chain triglycerides and it was not regiospecific; the lipase demonstrated naturally occurring stability in different organic solvents with concentrations ranging from 30 to 70%, including good thermal stability in 30% organic solvent solution. Even though strain P. aeruginosa ATCC 27853 was not isolated from extreme environment it showed activity in organic solvent suggesting that this lipase is suitable for variety of applications, including reactions in water restricted medium and bioremediation of contaminations by organic solvents.",
journal = "Journal of Basic Microbiology",
title = "Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853",
volume = "49",
number = "5",
pages = "452-462",
doi = "10.1002/jobm.200800229"
}

Izrael‑Živković, L., Gojgić-Cvijović, G., Gopcevic, K.R., Vrvić, M.,& Karadžić, I.. (2009). Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853. in Journal of Basic Microbiology, 49(5), 452-462.
https://doi.org/10.1002/jobm.200800229

Izrael‑Živković L, Gojgić-Cvijović G, Gopcevic K, Vrvić M, Karadžić I. Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853. in Journal of Basic Microbiology. 2009;49(5):452-462.
doi:10.1002/jobm.200800229 .

Izrael‑Živković, Lidija, Gojgić-Cvijović, Gordana, Gopcevic, K.R., Vrvić, Miroslav, Karadžić, Ivanka, "Enzymatic characterization of 30 kDa lipase from Pseudomonas aeruginosa ATCC 27853" in Journal of Basic Microbiology, 49, no. 5 (2009):452-462,
https://doi.org/10.1002/jobm.200800229 . .